dbPTM

CETN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CETN2_HUMAN
UniProt AC	P41208
Protein Name	Centrin-2
Gene Name	CETN2
Organism	Homo sapiens (Human).
Sequence Length	172
Subcellular Localization	Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Nucleus . Centrosome of S-phase, interphase and mitotic cells.
Protein Description	Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110.; Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with RAD23B appears to stabilize XPC. In vitro, stimulates DNA binding of the XPC:RAD23B dimer.; The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair.; Component of the TREX-2 complex (transcription and export complex 2), composed of at least ENY2, GANP, PCID2, SEM1, and either centrin CETN2 or CETN3. [PubMed: 22307388 The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery]
Protein Sequence	MASNFKKANMASSSQRKRMSPKPELTEEQKQEIREAFDLFDADGTGTIDVKELKVAMRALGFEPKKEEIKKMISEIDKEGTGKMNFGDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVSEQEFLRIMKKTSLY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASNFKKAN ------CCCHHHHHC	17.12	22814378
3	Phosphorylation	-----MASNFKKANM -----CCCHHHHHCC	41.31	26074081
6	Ubiquitination	--MASNFKKANMASS --CCCHHHHHCCCCH	56.05	24816145
6	Acetylation	--MASNFKKANMASS --CCCHHHHHCCCCH	56.05	30587599
6	Methylation	--MASNFKKANMASS --CCCHHHHHCCCCH	56.05	-
7	Methylation	-MASNFKKANMASSS -CCCHHHHHCCCCHH	40.64	-
12	Phosphorylation	FKKANMASSSQRKRM HHHHCCCCHHHHHCC	21.54	26074081
13	Phosphorylation	KKANMASSSQRKRMS HHHCCCCHHHHHCCC	22.43	26074081
14	Phosphorylation	KANMASSSQRKRMSP HHCCCCHHHHHCCCC	31.35	25849741
17	Ubiquitination	MASSSQRKRMSPKPE CCCHHHHHCCCCCCC	44.83	23000965
19	Sulfoxidation	SSSQRKRMSPKPELT CHHHHHCCCCCCCCC	10.11	21406390
20	Phosphorylation	SSQRKRMSPKPELTE HHHHHCCCCCCCCCH	33.53	29255136
22	Ubiquitination	QRKRMSPKPELTEEQ HHHCCCCCCCCCHHH	43.76	23000965
22	Sumoylation	QRKRMSPKPELTEEQ HHHCCCCCCCCCHHH	43.76	28112733
26	Phosphorylation	MSPKPELTEEQKQEI CCCCCCCCHHHHHHH	35.50	20201521
30	Ubiquitination	PELTEEQKQEIREAF CCCCHHHHHHHHHHH	53.85	29967540
54	Ubiquitination	TIDVKELKVAMRALG EEEHHHHHHHHHHCC	29.10	29967540
65	Ubiquitination	RALGFEPKKEEIKKM HHCCCCCCHHHHHHH	66.67	29967540
72	Sulfoxidation	KKEEIKKMISEIDKE CHHHHHHHHHHHCCC	3.28	21406390
78	Ubiquitination	KMISEIDKEGTGKMN HHHHHHCCCCCCCCC	64.80	-
103	Ubiquitination	KMSEKDTKEEILKAF HCCCCCCHHHHHHHH	64.58	22817900
108	Ubiquitination	DTKEEILKAFKLFDD CCHHHHHHHHHHCCC	58.39	23000965
111	Ubiquitination	EEILKAFKLFDDDET HHHHHHHHHCCCCCC	53.77	23000965
118	Phosphorylation	KLFDDDETGKISFKN HHCCCCCCCCCCHHH	51.25	-
120	Acetylation	FDDDETGKISFKNLK CCCCCCCCCCHHHHH	42.47	26051181
120	Ubiquitination	FDDDETGKISFKNLK CCCCCCCCCCHHHHH	42.47	23000965
122	Phosphorylation	DDETGKISFKNLKRV CCCCCCCCHHHHHHH	33.38	24719451
124	Acetylation	ETGKISFKNLKRVAK CCCCCCHHHHHHHHH	55.36	25953088
124	Ubiquitination	ETGKISFKNLKRVAK CCCCCCHHHHHHHHH	55.36	23000965
127	Ubiquitination	KISFKNLKRVAKELG CCCHHHHHHHHHHHH	54.97	23000965
131	Ubiquitination	KNLKRVAKELGENLT HHHHHHHHHHHHCCC	51.09	29967540
138	Phosphorylation	KELGENLTDEELQEM HHHHHCCCHHHHHHH	53.60	22817900
158	Phosphorylation	RDGDGEVSEQEFLRI CCCCCCCCHHHHHHH	29.29	27499020
167	Ubiquitination	QEFLRIMKKTSLY-- HHHHHHHHHHCCC--	50.99	29967540
170	Phosphorylation	LRIMKKTSLY----- HHHHHHHCCC-----	34.25	11279195

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
138	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
158	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
170	S	Phosphorylation	Kinase	AURKA	O14965	GPS
170	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
170	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
170	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CETN2_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of CETN2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SFI1_HUMAN	SFI1	physical	14504268
XPC_HUMAN	XPC	physical	11279143
XPC_HUMAN	XPC	physical	22939629
NAA40_HUMAN	NAA40	physical	22939629
SNUT2_HUMAN	USP39	physical	22939629
ANM6_HUMAN	PRMT6	physical	21988832
PNMA5_HUMAN	PNMA5	physical	25416956
SGSM1_HUMAN	SGSM1	physical	25416956
POC5_HUMAN	POC5	physical	25416956
IMDH2_HUMAN	IMPDH2	physical	26344197
AP2S1_HUMAN	AP2S1	physical	26638075
BTF3_HUMAN	BTF3	physical	26638075
TCPB_HUMAN	CCT2	physical	26638075
TCPG_HUMAN	CCT3	physical	26638075
TCPD_HUMAN	CCT4	physical	26638075
TCPE_HUMAN	CCT5	physical	26638075
TCPZ_HUMAN	CCT6A	physical	26638075
TCPH_HUMAN	CCT7	physical	26638075
COPB2_HUMAN	COPB2	physical	26638075
DEP1B_HUMAN	DEPDC1B	physical	26638075
DVL1_HUMAN	DVL1	physical	26638075
LRRC2_HUMAN	LRRC2	physical	26638075
MS18A_HUMAN	MIS18A	physical	26638075
PDCD5_HUMAN	PDCD5	physical	26638075
PKN2_HUMAN	PKN2	physical	26638075
POC5_HUMAN	POC5	physical	26638075
RD23B_HUMAN	RAD23B	physical	26638075
SPART_HUMAN	SPG20	physical	26638075
TCPA_HUMAN	TCP1	physical	26638075
TTF2_HUMAN	TTF2	physical	26638075
XPC_HUMAN	XPC	physical	26638075
ZC3HF_HUMAN	ZC3H15	physical	26638075
UBP44_HUMAN	USP44	physical	27880911
RD23B_HUMAN	RAD23B	physical	27880911
XPC_HUMAN	XPC	physical	27880911

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CETN2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-26, AND MASSSPECTROMETRY.	17081983 [Abstract]